Release of glucose-mediated catabolite repression due to a defect in the membrane fraction of phosphoenolpyruvate: mannose phosphotransferase system in Pediococcus halophilus

Keietsu Abe, Kinji Uchida

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)

Abstract

A spontaneous mutant 9R-4 resistant to 2-deoxyglucose (2DG) was derived from a wild-type strain Pediococcus halophilus I-13. Phosphoenolpyruvate (PEP)-dependent glucose-6-phosphate formation by the permeabilized 9R-4 cells was < 5% of that observed with the parent I-13. In vitro complementation of PEP-dependent 2DG-6-phosphate formation was assayed with combination of the cytoplasmic and membrane fractions prepared from the I-13 and the mutants (9R-4, and X-160 isolated from nature), which were defective in PEP: mannose phosphotransferase system (man:PTS). The defects in man:PTS of both the strain 9R-4 and X-160 were restricted to the membrane fraction (e.g. EIIman), not to the cytoplasmic one. Kinetic studies on the glucose transport with intact cells and iodoacetate-treated cells also supported the presence of two distinct transport systems in this bacterium as follows: (i) The wild-type I-13 possessed a high-affinity man:PTS (Km=11 μM) and a low-affinity proton motive force driven glucose permease (GP) (Km=170 μM). (ii) Both 9R-4 and X-160 had only the low-affinity system (Km=181 μM for 9R-4, 278 μM for X-160). In conclusion, a 2DG-induced selective defect in the membrane component (EIIman) of the man:PTS could partially release glucose-mediated catabolite repression but not frutose-mediated catabolite repression in soy pediococci.

Original languageEnglish
Pages (from-to)517-520
Number of pages4
JournalArchives of Microbiology
Volume155
Issue number6
DOIs
Publication statusPublished - 1991 Jun 1
Externally publishedYes

Keywords

  • Catabolite repression
  • EnzymeII
  • Glucose permease
  • Glucose transport
  • Membrane
  • Pediococcus halophilus
  • Phosphotransferase

ASJC Scopus subject areas

  • Microbiology

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